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The extreme N‐terminus of the calcitonin‐like receptor contributes to the selective interaction with adrenomedullin or calcitonin gene‐related peptide
Author(s) -
Koller Daniela,
Born Walter,
Leuthäuser Kerstin,
Flühmann Beat,
McKinney R.Anne,
Fischer Jan A,
Muff Roman
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03585-8
Subject(s) - calcitonin receptor , enzyme linked receptor , receptor , adrenomedullin , 5 ht5a receptor , calcitonin gene related peptide , interleukin 21 receptor , estrogen related receptor gamma , protease activated receptor 2 , chemistry , gabbr1 , nuclear receptor co repressor 1 , microbiology and biotechnology , biochemistry , endocrinology , biology , gene , nuclear receptor , neuropeptide , transcription factor
The calcitonin (CT)‐like (CL) receptor is a CT gene‐related peptide (CGRP) receptor or an adrenomedullin (AM) receptor when co‐expressed with receptor‐activity‐modifying proteins (RAMP) 1 or 2, respectively. The CL receptor shows 57% overall sequence identity with the CT receptor, but the homology is much lower in the extreme N‐terminus. An N‐terminal deletion mutant of the human (h) CL receptor (Δ18‐hCL) and a chimeric receptor consisting of the N‐terminal amino acids of the porcine (p) CT receptor fused to the Δ18‐hCL receptor (pCT–hCL) were therefore analyzed. The Δ18‐hCL receptor function was abolished when co‐expressed with RAMP1 or ‐2. The pCT–hCL receptor was a fully functional CGRP receptor when co‐expressed with RAMP1, but the RAMP2‐dependent AM receptor function was impaired. Limited sequence similarities in the N‐terminus of the pCT and the hCL receptors rescue CGRP but not AM receptor binding and signalling.